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Molten globule intermediates and protein folding.

H Christensen¹, R H Pain

¹Department of Biochemistry and Genetics, University of Newcastle upon Tyne, United Kingdom.

European Biophysics Journal : EBJ

|January 1, 1991

Summary

The molten globule state, a compact protein intermediate with secondary structure, is crucial for understanding protein folding pathways. Its characteristics and relationship to transient folding intermediates are clarified.

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Area of Science:

Biochemistry
Structural Biology
Protein Dynamics

Background:

The molten globule state represents a key intermediate in protein folding.
It exhibits secondary structure and high conformational mobility, distinct from the native state.
Stable and transient molten globule intermediates share properties but can differ in Stokes radius.

Purpose of the Study:

To discuss the concept and characteristics of the molten globule state.
To compare stable and transient molten globule intermediates.
To review experimental evidence on early protein folding stages.

Main Methods:

Literature review of experimental evidence on protein folding.
Comparison of properties of different intermediate states.
Analysis of the temporal relationship between collapse and secondary structure formation.

Main Results:

Molten globule intermediates possess secondary structure and mobility.
Stable and transient intermediates share features but can be distinguished.
Early folding involves polypeptide chain collapse preceding secondary structure formation.

Conclusions:

The term "molten globule" is recommended for states meeting specific structural criteria.
Understanding molten globule states is vital for protein folding research.
Further investigation is needed for stable intermediates on folding pathways.

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